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Literature summary for 4.2.3.5 extracted from

  • Rauch, G.; Ehammer, H.; Bornemann, S.; Macheroux, P.
    Mutagenic analysis of an invariant aspartate residue in chorismate synthase supports its role as an active site base (2007), Biochemistry, 46, 3768-3774.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Neurospora crassa

Protein Variants

Protein Variants Comment Organism
D367A comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower Neurospora crassa
D367N comparable to the wild-type enzyme with respect to substrate and cofactor binding, but activity significantly lower Neurospora crassa

Inhibitors

Inhibitors Comment Organism Structure
dioxygen inactivation Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-enolpyruvylshikimate 3-phosphate
-
Neurospora crassa chorismate + phosphate
-
?

Synonyms

Synonyms Comment Organism
chorismate synthase
-
Neurospora crassa

Cofactor

Cofactor Comment Organism Structure
FMN essential for catalytic activity Neurospora crassa